Alpha-1-microglobulin/bikunin precursor

Protein AMBP is a protein that in humans is encoded by the AMBP gene.[5][6][7]

AMBP
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1BIK, 3QKG, 4ES7, 4U30
Identifiers
Aliases	AMBP, A1M, EDC1, HCP, HI30, IATIL, ITI, ITIL, ITILC, UTI, alpha-1-microglobulin/bikunin precursor
External IDs	OMIM: 176870 MGI: 88002 HomoloGene: 1234 GeneCards: AMBP
Gene location (Human) Chr. Chromosome 9 (human)[1] Band 9q32 Start 114,060,127 bp[1] End 114,078,328 bp[1]
Gene location (Mouse) Chr. Chromosome 4 (mouse)[2] Band 4 B3|4 33.96 cM Start 63,143,275 bp[2] End 63,154,799 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • peptidase inhibitor activity • calcium channel inhibitor activity • protein homodimerization activity • calcium oxalate binding • GO:0001948 protein binding • heme binding • serine-type endopeptidase inhibitor activity • small molecule binding • IgA binding Cellular component • blood microparticle • intracellular membrane-bounded organelle • cell membrane • extracellular region • cell surface • extracellular exosome • extracellular • extracellular matrix • collagen-containing extracellular matrix Biological process • negative regulation of peptidase activity • female pregnancy • receptor-mediated endocytosis • negative regulation of JNK cascade • heme catabolic process • negative regulation of immune response • cell adhesion • protein catabolic process • protein-chromophore linkage • GO:0022415 viral process • negative regulation of endopeptidase activity Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	259	11699
Ensembl	ENSG00000106927	ENSMUSG00000028356
UniProt	P02760	Q07456
RefSeq (mRNA)	NM_001633	NM_007443
RefSeq (protein)	NP_001624	NP_031469
Location (UCSC)	Chr 9: 114.06 – 114.08 Mb	Chr 4: 63.14 – 63.15 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Interactions

Alpha-1-microglobulin/bikunin precursor has been shown to interact with CD79A.[8][9]

See also

• Inter-alpha-trypsin inhibitor
• Alpha-1-microglobulin

References

1. GRCh38: Ensembl release 89: ENSG00000106927 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000028356 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Vetr H, Gebhard W (1990). "Structure of the human alpha 1-microglobulin-bikunin gene". Biol. Chem. Hoppe-Seyler. 371 (12): 1185–96. doi:10.1515/bchm3.1990.371.2.1185. PMID 1708673.
6. Salier JP, Simon D, Rouet P, Raguenez G, Muscatelli F, Gebhard W, Guenet JL, Mattei MG (Dec 1992). "Homologous chromosomal locations of the four genes for inter-alpha-inhibitor and pre-alpha-inhibitor family in human and mouse: assignment of the ancestral gene for the lipocalin superfamily". Genomics. 14 (1): 83–8. doi:10.1016/S0888-7543(05)80287-3. PMID 1385302.
7. "Entrez Gene: AMBP alpha-1-microglobulin/bikunin precursor".
8. Grubb AO, López C, Tejler L, Mendez E (December 1983). "Isolation of human complex-forming glycoprotein, heterogeneous in charge (protein HC), and its IgA complex from plasma. Physiochemical and immunochemical properties, normal plasma concentration". J. Biol. Chem. 258 (23): 14698–707. PMID 6196366.
9. Berggård T, Thelin N, Falkenberg C, Enghild JJ, Akerström B (May 1997). "Prothrombin, albumin and immunoglobulin A form covalent complexes with alpha1-microglobulin in human plasma". Eur. J. Biochem. 245 (3): 676–83. doi:10.1111/j.1432-1033.1997.00676.x. PMID 9183005.

Further reading

• Akerström B, Lögdberg L, Berggård T, Osmark P, Lindqvist A (2000). "alpha(1)-Microglobulin: a yellow-brown lipocalin". Biochim. Biophys. Acta. 1482 (1–2): 172–84. doi:10.1016/S0167-4838(00)00157-6. PMID 11058759.
• Kobayashi H, Suzuki M, Hirashima Y, Terao T (2003). "The protease inhibitor bikunin, a novel anti-metastatic agent". Biol. Chem. 384 (5): 749–54. doi:10.1515/BC.2003.083. PMID 12817471. S2CID 38608465.
• Ekström B, Berggård I (1977). "Human alpha1-microglobulin. Purification procedure, chemical and physiochemical properties". J. Biol. Chem. 252 (22): 8048–57. PMID 72071.
• Escribano J, Lopex-Otin C, Hjerpe A, Grubb A, Mendez E (1990). "Location and characterization of the three carbohydrate prosthetic groups of human protein HC". FEBS Lett. 266 (1–2): 167–70. doi:10.1016/0014-5793(90)81531-R. PMID 1694784. S2CID 36320110.
• Diarra-Mehrpour M, Bourguignon J, Sesboüé R, Salier JP, Léveillard T, Martin JP (1990). "Structural analysis of the human inter-alpha-trypsin inhibitor light-chain gene". Eur. J. Biochem. 191 (1): 131–9. doi:10.1111/j.1432-1033.1990.tb19102.x. PMID 1696200.
• Gebhard W, Schreitmüller T, Vetr H, Wachter E, Hochstrasser K (1990). "Complementary DNA and deduced amino acid sequences of procine alpha 1-microglobulin and bikunin". FEBS Lett. 269 (1): 32–6. doi:10.1016/0014-5793(90)81112-2. PMID 1696914. S2CID 84271910.
• Falkenberg C, Grubb A, Akerström B (1990). "Isolation of rat serum alpha 1-microglobulin. Identification of a complex with alpha 1-inhibitor-3, a rat alpha 2-macroglobulin homologue". J. Biol. Chem. 265 (27): 16150–7. PMID 1697852.
• Nazimova SV, Akulenko IV, Zaĭtseva IV, Zaraĭskiĭ EI, Posiseeva LV (1990). "[Immunoenzyme analysis of placenta-specific alpha(1)-microglobulin in the blood serum in normal and pathological pregnancy]". Akush Ginekol (Mosk) (7): 70–2. PMID 1700638.
• Escribano J, Grubb A, Calero M, Méndez E (1991). "The protein HC chromophore is linked to the cysteine residue at position 34 of the polypeptide chain by a reduction-resistant bond and causes the charge heterogeneity of protein HC". J. Biol. Chem. 266 (24): 15758–63. PMID 1714898.
• Enghild JJ, Salvesen G, Hefta SA, Thøgersen IB, Rutherfurd S, Pizzo SV (1991). "Chondroitin 4-sulfate covalently cross-links the chains of the human blood protein pre-alpha-inhibitor". J. Biol. Chem. 266 (2): 747–51. PMID 1898736.
• Reisinger P, Hochstrasser K, Albrecht GJ, Lempart K, Salier JP (1985). "Human inter-alpha-trypsin inhibitor: localization of the Kunitz-type domains in the N-terminal part of the molecule and their release by a trypsin-like proteinase". Biol. Chem. Hoppe-Seyler. 366 (5): 479–83. doi:10.1515/bchm3.1985.366.1.479. PMID 2408638.
• Bourguignon J, Diarra-Mehrpour M, Sesboüé R, Frain M, Sala-Trepat JM, Martin JP, Salier JP (1985). "Human inter-alpha-trypsin-inhibitor: characterization and partial nucleotide sequencing of a light chain-encoding cDNA". Biochem. Biophys. Res. Commun. 131 (3): 1146–53. doi:10.1016/0006-291X(85)90210-4. PMID 2413856.
• Méndez E, Fernández-Luna JL, Grubb A, Leyva-Cobián F (1986). "Human protein HC and its IgA complex are inhibitors of neutrophil chemotaxis". Proc. Natl. Acad. Sci. U.S.A. 83 (5): 1472–5. doi:10.1073/pnas.83.5.1472. PMC 323098. PMID 2419908.
• Traboni C, Cortese R (1986). "Sequence of a full length cDNA coding for human protein HC (alpha 1 microglobulin)". Nucleic Acids Res. 14 (15): 6340. doi:10.1093/nar/14.15.6340. PMC 311643. PMID 2428011.
• Kaumeyer JF, Polazzi JO, Kotick MP (1986). "The mRNA for a proteinase inhibitor related to the HI-30 domain of inter-alpha-trypsin inhibitor also encodes alpha-1-microglobulin (protein HC)". Nucleic Acids Res. 14 (20): 7839–50. doi:10.1093/nar/14.20.7839. PMC 311818. PMID 2430261.
• Zaraĭskiĭ EI, Nazimova SV, Olefirenko GA, Pchelkina ZM, Petrunin DD, Tatarinov IuS, Fuks BB (1990). "[Immunoenzyme analysis of placenta-specific alpha 1-microglobulin in the serum of blood donors]". Vopr. Med. Khim. 35 (5): 130–2. PMID 2482577.
• Schreitmüller T, Hochstrasser K, Reisinger PW, Wachter E, Gebhard W (1987). "cDNA cloning of human inter-alpha-trypsin inhibitor discloses three different proteins". Biol. Chem. Hoppe-Seyler. 368 (8): 963–70. doi:10.1515/bchm3.1987.368.2.963. PMID 3663330.
• Morii M, Travis J (1985). "The reactive site of human inter-alpha-trypsin inhibitor is in the amino-terminal half of the protein". Biol. Chem. Hoppe-Seyler. 366 (1): 19–21. doi:10.1515/bchm3.1985.366.1.19. PMID 3890890.

External links

• The MEROPS online database for peptidases and their inhibitors: LI02-001